Ontology highlight
ABSTRACT:
SUBMITTER: Russell RJ
PROVIDER: S-EPMC2584702 | biostudies-literature | 2008 Nov
REPOSITORIES: biostudies-literature
Russell Rupert J RJ Kerry Philip S PS Stevens David J DJ Steinhauer David A DA Martin Stephen R SR Gamblin Steven J SJ Skehel John J JJ
Proceedings of the National Academy of Sciences of the United States of America 20081112 46
The influenza surface glycoprotein hemagglutinin (HA) is a potential target for antiviral drugs because of its key roles in the initial stages of infection: receptor binding and the fusion of virus and cell membranes. The structure of HA in complex with a known inhibitor of membrane fusion and virus infectivity, tert-butyl hydroquinone (TBHQ), shows that the inhibitor binds in a hydrophobic pocket formed at an interface between HA monomers. Occupation of this site by TBHQ stabilizes the neutral ...[more]